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© Marie Prévost, Institut Pasteur
Image of a portion of a Xenopus oocyte expressing a channel receptor.
Publication : European journal of pharmacology

Molecular characterization of the specificity of interactions of various neurotoxins on two distinct nicotinic acetylcholine receptors

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in European journal of pharmacology - 30 Mar 2000

Servent D, Antil-Delbeke S, Gaillard C, Corringer PJ, Changeux JP, Ménez A

Link to Pubmed [PMID] – 10771013

Eur. J. Pharmacol. 2000 Mar;393(1-3):197-204

Snake curaremimetic toxins are currently classified as short-chain and long-chain toxins according to their size and their number of disulfide bonds. All these toxins bind with high affinity to muscular-type nicotinic acetylcholine receptor, whereas only long toxins recognize the alpha7 receptor with high affinity. On the basis of binding experiments with Torpedo or neuronal alpha7 receptors using wild-type and mutated neurotoxins, we characterized the molecular determinants involved in these different recognition processes. The functional sites by which long and short toxins interact with the muscular-type receptor include a common core of highly conserved residues and residues that are specific to each of toxin families. Furthermore, the functional sites through which alpha-cobratoxin, a long-chain toxin, interacts with muscular and alpha7 receptors share similarities but also marked differences. Our results reveal that the three-finger fold toxins have evolved toward various specificities by displaying distinct functional sites.

http://www.ncbi.nlm.nih.gov/pubmed/10771013